threonine

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Related to Phosphothreonine: Phosphotyrosine

thre·o·nine

 (thrē′ə-nēn′, -nĭn)
n.
A colorless crystalline amino acid, C4H9NO3, that is obtained from the hydrolysis of protein and is an essential component of human nutrition.

[Probably from threose, a kind of sugar (alteration of erythrose : erythro- + -ose) + -ine.]

threonine

(ˈθriːəˌniːn; -nɪn)
n
(Biochemistry) an essential amino acid that occurs in certain proteins
[C20 threon-, probably from Greek eruthron, from eruthros red (see erythro-) + -ine2]

thre•o•nine

(ˈθri əˌnin, -nɪn)

n.
an essential amino acid, CH3CHOHCH(NH2)COOH, obtained by the hydrolysis of proteins. Symbol: T Abbr.: Thr
[1936; threon- (alter. of Greek erythrón, neuter of erythrós red; see erythro-) + -ine2]

thre·o·nine

(thrē′ə-nēn′)
An essential amino acid. See more at amino acid.
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.threonine - a colorless crystalline amino acid found in protein; occurs in the hydrolysates of certain proteins; an essential component of human nutrition
essential amino acid - an amino acid that is required by animals but that they cannot synthesize; must be supplied in the diet
Translations
Threonin
thréonine
treonina

threonine

n treonina
References in periodicals archive ?
Among the important functions predicted for OGG1 proteins were LIG_BRCT_BRCA1_1 instances of Phosphopeptide motif which directly interacts with the BRCT (carboxy-terminal) domain of the breast cancer gene BRCA1, LIG_FHA_2 of Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the replication fork, and MOD_TYR_ITSM of the CD150 subfamily of receptors that bind to and are regulated by SH2 adaptor molecule.
Since Western blotting is specific to phosphoserine, the approximately 130 and 80 kDa proteins stained by ProQ Diamond, not Western blotting, may contain only phosphothreonine (phospho-Thr) and/or phosphotyrosine (phosphoTyr) residues.
PTEN contains an N-terminal phosphatase domain that can dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine within highly acidic substrates, although with weak catalytic activity.

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